BRCA2: Shining light on the regulation of DNA-binding selectivity by RAD51 - PubMed (original) (raw)

Editorial

BRCA2: Shining light on the regulation of DNA-binding selectivity by RAD51

Aura Carreira et al. Cell Cycle. 2009.

No abstract available

Figures

Figure 1

(A) Schematic representation of BRCA2 protein showing its functional domains. H, helical domain; OB, oligonucleotide-binding fold; NLS, nuclear localization signal. (B) Molecular surface and ribbon representation of RAD51 bound to BRC4 (PDB code 1n0w). RAD51 is shown in blue and BRC4 in orange. The highly conserved interacting region of BRC4 is highlighted in red. (C) Illustration of the DNA binding domain structure of mouse BRCA2 DBD-DSS1 (PDB code 1MIU). The helical domain is shown in yellow, and OB 1, 2 and 3 are shown in red, blue and orange, respectively. DSS1 protein is shown in green. (D) Model for the function of BRCA2 in the repair of DNA breaks. Through its DNA binding domain, BRCA2 targets RAD51 to the dsDNA-ssDNA junction of a resected DSB. Using its BRC repeats, BRCA2 directs RAD51 onto the ssDNa and blocks assembly onto dsDNa. This interaction likely provides a nucleus for nascent ATP-RAD51 filament formation. Subsequent growth of the nucleoprotein filament from this nucleus will displace RPA. Eventually, the RAD51-ssDNA filament will pair with an intact copy of the chromosome to continue the steps of DNA repair (not shown).

References

1. Wooster R, et al. N Engl J Med. 2003;348:2339–47. - PubMed
1. Bianco PR, et al. Front Biosci. 1998;3:570–603. - PubMed
1. Wong AKC, et al. J Biol Chem. 1997;272:31941–4. - PubMed
1. Xia B, et al. Mol Cell. 2006;22:719–29. - PubMed
1. Hughes-Davies L, et al. Cell. 2003;115:523–35. - PubMed

BRCA2: Shining light on the regulation of DNA-binding selectivity by RAD51 - PubMed (original) (raw)